Leuconostoc citrovorumの菌体内プロテア-ゼの活性阻害剤ならびに賦活剤〔英文〕

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In the present study, the intracellular protease of Leuconostoc citrovorum was purified by ammonium precipitation and by Sephadex column and DEAE-cellulose column chromatography. Activity of the purified enzyme was progrssively inhibited with increasing of p-chloromercuribenzoate and iodoacetate, but not by o-phenanthroline and diisopropylfluorophosphate. This fact strongly suggest that a free sulfhydyl group(s) is required for activity. The possible involvement of this functional group, then, determined by treating the enzyme with iodine and/or glutathione. As results, activity of the enzyme was reactivated considerably by glutathione, and addition of glutathione to iodine oxidized enzyme resulted in 73.7% reactivity, whereas iodine oxidation of the enzyme resulted in 52.6% reduction in activity.
信州大学農学部の論文